Structure study of osteostatin PTHrP[Thr107](107-139)

Biochim Biophys Acta. 1999 Jun 15;1432(1):64-72. doi: 10.1016/s0167-4838(99)00078-3.


The structure of chicken osteostatin or parathyroid hormone-related protein (PTHrP) (residues 107-139) containing an Ala/Thr substitution at the N-terminus was studied using two-dimensional proton NMR spectroscopy in an aqueous environment. Osteostatin is a separate circulating domain responsible for a range of activities related to the modulation of bone formation as well as keratinocyte proliferation. Anti-mitogenic properties of osteostatin have been detected in breast cancer cells and cytosolic calcium is used by osteostatin to signal in some neurons through a non-PTH receptor, unlike the separate circulating N-terminal domain. A structural basis for the activity is presented with particular emphasis given to the conformation of the bioactive segment 107-111, forming part of a finger-like projection capable of binding to the non-PTH receptor both in the presence and absence of the remainder of the molecule which appears simply to act as a largely globular carrier.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Magnetic Resonance Spectroscopy / methods
  • Models, Molecular
  • Molecular Sequence Data
  • Parathyroid Hormone / chemistry*
  • Parathyroid Hormone-Related Protein*
  • Peptide Fragments / chemistry*


  • Parathyroid Hormone
  • Parathyroid Hormone-Related Protein
  • Peptide Fragments
  • parathyroid hormone-related protein (107-139)amide